Investigation of the binding of perfluorocarboxylates to a model serum protein: A comparison of analytical methods

ANYL 155

Laura A MacManus-Spencer, macmanul@union.edu1, Monica L Tse1, Heather Bischel2, and Richard G Luthy, luthy@stanford.edu2. (1) Department of Chemistry, Union College, Science & Engineering, 807 Union Street, Schenectady, NY 12308, (2) Department of Civil and Environmental Engineering, Stanford University, Terman Engineering Center, Stanford, CA 94305-4020
In recent years, perfluorochemicals have emerged as globally pervasive contaminants that are persistent, bioaccumulative, and toxic. Perfluorocarboxylates (PFCAs) with 7-12 perfluoroalkyl carbons accumulate in the liver and blood of aquatic and terrestrial organisms. PFCA-protein interactions may contribute to this accumulation, and the binding of PFCAs to proteins may interfere with normal function. In this study, the interactions between PFCAs with 7-10 perfluoroalkyl carbons and a model serum protein, bovine serum albumin (BSA), were examined using several experimental approaches. The native absorbance and fluorescence of BSA, 19F NMR, and surface tension measurements were used to investigate PFCA-BSA binding over a broad concentration range. Fluorescence and absorbance measurements indicate that PFCA-BSA interactions alter the conformation of BSA. Fluorescence and 19F NMR were used to determine binding constants for PFCA-BSA complexes. Surface tension measurements suggest complex formation at high PFCA concentrations, possibly with PFCA micelles.
 

Environmental Chemistry
8:55 AM-11:55 AM, Tuesday, April 8, 2008 Morial Convention Center -- Rm. 335, Oral

Division of Analytical Chemistry

The 235th ACS National Meeting, New Orleans, LA, April 6-10, 2008